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- W2000591892 abstract "Heat-shock protein 70 (Hsp70), one of the major molecular chaperones, has been shown to play a central role in many cellular processes. Heat-shock protein 40 (Hsp40) works as a co-chaperone for Hsp70. Hsp40, bound by unfolded polypeptide, can interact directly with Hsp70 to stimulate the ATPase activity of Hsp70. Hsp40 can also bind to unfolded polypeptides and prevent them from aggregating in vitro , thus acting as an independent molecular chaperone. The S. cerevisiae Hsp40 Sis1 C-terminal peptide-binding domain has been crystallized. The crystals diffract to 2.7 Å and belong to space group P 4 1 2 1 2 or P 4 3 2 1 2 with a = 73.63, c = 80.16 Å. The structure determination by the MAD method is under way." @default.
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- W2000591892 date "1999-06-01" @default.
- W2000591892 modified "2023-10-16" @default.
- W2000591892 title "Purification, crystallization and preliminary X-ray crystallographic studies of <i>S. cerevisiae</i> Hsp40 Sis1" @default.
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- W2000591892 doi "https://doi.org/10.1107/s090744499900476x" @default.
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